Abstract
A general ice block is made of infinite number of single ice crystals, whose embryos are generated at the
moment of freezing. Antifreeze protein (AFP) or antifreeze glycoprotein (AFGP) accumulates on the specific
surfaces of such embryonic ice crystals, which suppresses their ice growth and stabilizes a supercooled
solution. This mechanism has been thought to provide cold-tolerance for an organism, and realize new
freezing preservation techniques of various water-containing materials, such as processed foods, gels,
noodles, doughs, seeds, fruits, vegetables, ice creams, polymers, medicines, cosmetics, cells, tissues, and
organs. If the proteins can make the ice crystal size ultimately small, they will significantly improve the
effectiveness of the preservations. In addition, many AFPs bind to the lipid bilayer to prolong lifetime of
cells under hypothermic condition (+4°C), for which applicability to unfrozen, short-term cell preservation
can be expected. The author has therefore been tried to clarify the functional mechanism of AFPs and AFGP,
and further developed their mass-preparation method to find their usefulness in both industrial and medical
fields. This article provides advanced knowledge obtained through the works mainly performed by the
author.
